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. 2023 Oct 7;14:6271. doi: 10.1038/s41467-023-41862-x

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Structural similarity of human insulin (top left) and DILP5 (right), B-chains in grey, A-chains in coral, pale yellow—insulin’s B1-B6 N-terminus in the so-called R-state; bottom – the sequence alignment of human insulin, hIGF-1 (its C-domain is omitted here as not relevant for DILPs) and DILP5. b Functional homology and conservation of IIS axis in humans and Drosophila, with some representatives of the key and common downstream effector proteins. c Schematic representation of the domain organisation, and examples of some key structural conformers, of the hIR in the apo (far left) and its holo forms; yellow/green—hIR protomers, insulins in site 1/1’ in pink, insulins in site 2/2’ in blue; PDB IDs are given for some representative structures. d Comparison of the domain organisation of hIR and dmIR αβ protomers (based on the sequence alignment), and their sequence similarity (in %); in magenta—domains involved in insulin binding site 1/1’, in yellow—site 2/2’; dashed lines - disulfide bonds; dmIR has only two inter-ID domains -SS- bonds, as it does not have the equivalent of human Cys682 in this region.